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Database: UniProt
Entry: A0A556QJU8_9BACT
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ID   A0A556QJU8_9BACT        Unreviewed;       860 AA.
AC   A0A556QJU8;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:TSJ76924.1};
GN   ORFNames=FPL22_12465 {ECO:0000313|EMBL:TSJ76924.1};
OS   Rariglobus hedericola.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Rariglobus.
OX   NCBI_TaxID=2597822 {ECO:0000313|EMBL:TSJ76924.1, ECO:0000313|Proteomes:UP000315648};
RN   [1] {ECO:0000313|EMBL:TSJ76924.1, ECO:0000313|Proteomes:UP000315648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=53C-WASEF {ECO:0000313|EMBL:TSJ76924.1,
RC   ECO:0000313|Proteomes:UP000315648};
RA   Pitt A., Hahn M.W.;
RT   "Description of 53C-WASEF.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC       involved in the recovery of the cell from heat-induced damage, in
CC       cooperation with DnaK, DnaJ and GrpE. {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TSJ76924.1}.
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DR   EMBL; VMBG01000002; TSJ76924.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A556QJU8; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000315648; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017730; Chaperonin_ClpB.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000315648};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..150
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          409..503
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   860 AA;  95849 MW;  1C6FD325B0F5A360 CRC64;
     MDSNQLTQMS RQAVTDAQAE ARRRSHNEVE TWHLLHALLA QENGIVPALV EKLGLTTSAL
     QLAAERELDR LPKVSGSVDT SKVYVTQSVN EVLTRAEAEA KSLKDDFVSV EHLFLGLLDV
     AKPDALKNYF KSFGIERTKV LKSLKDLRGA QRVTTDNPET TYAALTKYGI DLVELAKKGK
     MDPVIGRDDE IRRTVRILSR KTKNNPVLIG EPGVGKTAIV EGLAQRIVRG DVPEGLKDKT
     IFSLDMGALV AGAKYRGEFE ERLKAVLNEV KQADGRIILF IDELHTIVGA GKSDGAMDAG
     NLLKPMLARG ELHCIGATTL DEYRQHIEKD AALERRFQPV MVEPPSVEDA ISILRGIRER
     FELHHGVRIQ DNALVAAVTL SNRYISDRFL PDKAIDLMDE ACAMIRTEMD SAPQELDALQ
     RRVLQLEIEE AALKLEKDDA SKHRLESLRK ELADARSQAA GLKAKWDKEK DSVNAVRAVR
     EQLDAARIEL EKAERNYDLN KLAELRHGKI PQLEAELKKS ETTAAKTELF KEEVSAEEIA
     EIVSKWSGVP VTRFVEGEKE KLLRLGEVLH ERVIGQDEAV TLATDAILRA RAGIKDPRRP
     VGSFLFLGPT GVGKTELAKT LAETLFDSEA ALVRIDMSEY MEKHSVSRLV GAPPGYIGYD
     EGGQLTEAVR RKPYAVILFD EIEKAHPDVF NILLQVLDDG RITDSQGRTI DFKNTVIILT
     SNLGSRYLIE GVTTDVIPES VRESVMAEVR KAFRPEFLNR IDETILFKPL TLEEITRIVD
     LLLADLNKRL LDRRVTVMLD KTAKAWVGEK GYDPVYGARP LKRFLQRQIE TKLARALIGG
     EVKDGAEVTF KVQGDELVIA
//
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